Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: implications for regulation of actin-myosin interaction.
about
Fatigue development in the finger flexor muscle differs between keyboard and mouse useMyosin light chain kinase and the role of myosin light chain phosphorylation in skeletal musclePhosphorylation of the regulatory light chain of myosin in striated muscle: methodological perspectivesBasal myosin light chain phosphorylation is a determinant of Ca2+ sensitivity of force and activation dependence of the kinetics of myocardial force developmentMyosin regulatory light chain phosphorylation attenuates cardiac hypertrophyThe significance of regulatory light chain phosphorylation in cardiac physiologyAcceleration of stretch activation in murine myocardium due to phosphorylation of myosin regulatory light chainEffect of viscosity on mechanics of single, skinned fibers from rabbit psoas muscle.The molecular effects of skeletal muscle myosin regulatory light chain phosphorylation.Activation kinetics of skinned cardiac muscle by laser photolysis of nitrophenyl-EGTA.Sarcomere lattice geometry influences cooperative myosin binding in muscle.Reduced force production during low blood flow to the heart correlates with altered troponin I phosphorylationAcidic residues comprise part of the myosin light chain-binding site on skeletal muscle myosin light chain kinase.The direct molecular effects of fatigue and myosin regulatory light chain phosphorylation on the actomyosin contractile apparatus.Phosphorylation-dependent power output of transgenic flies: an integrated study.Kinetics of thin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle: implications for regulation of muscle cInfluence of Ca2+ on force redevelopment kinetics in skinned rat myocardiumIsometric force redevelopment of skinned muscle fibers from rabbit activated with and without Ca2+Calmidazolium alters Ca2+ regulation of tension redevelopment rate in skinned skeletal muscleFunction of the N terminus of the myosin essential light chain of vertebrate striated muscle.Phosphorylation of myosin regulatory light chain eliminates force-dependent changes in relaxation rates in skeletal muscle.Force regulation by Ca2+ in skinned single cardiac myocytes of frogCalcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] in rabbit skeletal muscle.The effect of ATP analogs on posthydrolytic and force development steps in skinned skeletal muscle fibers.Regulation of skeletal muscle tension redevelopment by troponin C constructs with different Ca2+ affinities.Kinetic effects of myosin regulatory light chain phosphorylation on skeletal muscle contraction.Tension recovery in permeabilized rat soleus muscle fibers after rapid shortening and restretch.ACTN3 and MLCK genotype associations with exertional muscle damage.Essential "ankle" in the myosin lever arm.Regulatory light chain phosphorylation and N-terminal extension increase cross-bridge binding and power output in Drosophila at in vivo myofilament lattice spacingMultiple causes of fatigue during shortening contractions in rat slow twitch skeletal musclePositive inotropic effects of low dATP/ATP ratios on mechanics and kinetics of porcine cardiac muscleCharge replacement near the phosphorylatable serine of the myosin regulatory light chain mimics aspects of phosphorylation.X-ray diffraction studies of the thick filament in permeabilized myocardium from rabbit.Role of calcium sensitivity modulation in skeletal muscle performance.Considerations on the history dependence of muscle contraction.Calcium regulation of myosin-I tension sensingMyosin Light Chain Kinase (MLCK) Gene Influences Exercise Induced Muscle Damage during a Competitive MarathonTrading force for speed: why superfast crossbridge kinetics leads to superlow forcesMyosin light chain-2 mutation affects flight, wing beat frequency, and indirect flight muscle contraction kinetics in Drosophila.
P2860
Q23914753-45779878-CA78-4864-A0CA-0A95B1534F73Q24631228-C083E3A4-2F08-4352-BABD-63DC8817CDD4Q28078785-6B1EB6C0-4278-4B59-9B90-BAABAC082069Q28278986-9F27BBF2-704F-4025-A736-43F023CDD4FEQ28279821-307DF168-60FE-4FA6-89F1-0590585053DBQ28305925-6DF91DE6-C2AC-48EE-8271-2F392578206CQ28510291-6D391501-B19B-4293-AAC0-DD7FF29CD16AQ30447540-8FA591F5-F1D4-48B3-8135-83FBDB337AAFQ30489420-13B6FD3E-3E6E-4CB0-B993-3E59D4DFD1C3Q30827985-FD0ECBD2-17D8-4081-B704-4CE749E804F1Q33290825-91BC2FED-FFEA-4DFE-A8A9-A1CFC7906A42Q33641335-1D77592C-76E8-4E23-BC8B-568BAB037F33Q33720313-F6D9B60C-9334-4FA1-A2D7-F8F8A8C3643BQ33784312-21059A35-8382-4F13-AFEF-215106BA2D93Q33907968-4B3261E1-B515-4243-95A4-DF44C6EA77F9Q33947371-034B9B4C-2DD2-43AB-A7F5-3D590EB7C35DQ34017975-A8305D47-F0BC-4DE4-9D7F-3818E15123F1Q34018888-6288208A-5882-4A1A-9301-C6B209C1B509Q34041122-415D16C3-CC64-4FAF-A502-EEE7D37A55CFQ34128886-A251A298-2012-481A-BFC4-184AF01F1786Q34167129-40D46D02-C119-445C-A306-300DFBA23242Q34167624-E7024381-0AB4-4488-8FE1-A2F4E4B282B1Q34167632-29725E3B-73B4-46A7-ABD0-D3F3A6CA7980Q34168132-78388DE7-E699-49AF-B1F8-BB330DA9E5D1Q34170456-88BE28F0-B633-41B6-9422-315A1CA21B14Q34178329-1048F6A3-8DBD-4FD6-B414-54BCB715CA29Q34354124-34C80DDC-ABB6-466E-A4F3-E77D156C40DAQ34409729-5E9EA386-B31C-42F3-8657-8319DDF78EE0Q34471682-6E8BAB60-94A4-4B93-927B-E59AC3C14A70Q34771937-7E009B5E-3070-4D01-B09C-8753E7718EC2Q34971931-034621F5-051F-4B58-A492-51EF971DBBDBQ35012245-42DA96CC-EF4B-4987-9B6A-75AF5BD22EF4Q35053697-16EA4193-376D-4A2A-8056-39EC6BBD2071Q35121304-F303BCA3-D3F3-4B23-9F17-5574CE972AB6Q35582274-1D0D99B5-FEFD-4F26-AE14-E1EB04CC6AEEQ35625557-114C78DD-ACA8-47C3-A203-90C92B34145BQ36047360-974C2AB2-024A-46D0-8717-D316B075EEC7Q36092525-5FA47A0F-EC2C-4225-8CE5-A8EAE8095508Q36372409-2F79556D-2C8C-4A39-813B-6536D0B31991Q36532347-3C750629-B1B5-4DBB-9116-2E3C1F898512
P2860
Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: implications for regulation of actin-myosin interaction.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 1990
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Alteration of cross-bridge kin ...... n of actin-myosin interaction.
@en
Alteration of cross-bridge kin ...... n of actin-myosin interaction.
@nl
type
label
Alteration of cross-bridge kin ...... n of actin-myosin interaction.
@en
Alteration of cross-bridge kin ...... n of actin-myosin interaction.
@nl
prefLabel
Alteration of cross-bridge kin ...... n of actin-myosin interaction.
@en
Alteration of cross-bridge kin ...... n of actin-myosin interaction.
@nl
P2860
P356
P1476
Alteration of cross-bridge kin ...... n of actin-myosin interaction.
@en
P2093
H L Sweeney
P2860
P304
P356
10.1073/PNAS.87.1.414
P407
P577
1990-01-01T00:00:00Z